Review https://pubmed.ncbi.nlm.nih.gov/37360529/
. 2023 Jun 9;13:1217383.
doi: 10.3389/fcimb.2023.1217383.
eCollection 2023.
Role of E3 ubiquitin ligases and deubiquitinating enzymes in SARS-CoV-2 infection
Affiliations
Abstract
Ever since its emergence in 2019, COVID-19 has rapidly
disseminated worldwide, engendering a pervasive pandemic that has
profoundly impacted healthcare systems and the socio-economic milieu. A
plethora of studies has been conducted targeting its pathogenic virus,
SARS-CoV-2, to find ways to combat COVID-19. The ubiquitin-proteasome
system (UPS) is widely recognized as a crucial mechanism that regulates
human biological activities by maintaining protein homeostasis. Within
the UPS, the ubiquitination and deubiquitination, two reversible
modifications, of substrate proteins have been extensively studied and
implicated in the pathogenesis of SARS-CoV-2. The regulation of E3
ubiquitin ligases and DUBs(Deubiquitinating enzymes), which are key
enzymes involved in the two modification processes, determines the fate
of substrate proteins. Proteins associated with the pathogenesis of
SARS-CoV-2 may be retained, degraded, or even activated, thus affecting
the ultimate outcome of the confrontation between SARS-CoV-2 and the
host. In other words, the clash between SARS-CoV-2 and the host can be
viewed as a battle for dominance over E3 ubiquitin ligases and DUBs,
from the standpoint of ubiquitin modification regulation. This review
primarily aims to clarify the mechanisms by which the virus utilizes
host E3 ubiquitin ligases and DUBs, along with its own viral proteins
that have similar enzyme activities, to facilitate invasion,
replication, escape, and inflammation. We believe that gaining a better
understanding of the role of E3 ubiquitin ligases and DUBs in COVID-19
can offer novel and valuable insights for developing antiviral
therapies.
Keywords: COVID-19; E3 ubiquitin ligases; SARS-CoV-2; deubiquitinating enzymes (DUBs); ubiquitin.
Copyright © 2023 Zhao, Zhang, Yang, Zhou, Huang and Zhao.
Conflict of interest statement
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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